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ADAM9 (ADAM metallopeptidase domain 9 (meltrin gamma))

Identity

Other namesMDC9
Meltrin-gamma
MLTNG
MCMP
KIAA0021
HGNC (Hugo) ADAM9
LocusID (NCBI) 8754
Location 8p11.22
Location_base_pair Starts at 38854505 and ends at 38962779 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order TACC1 - PLEKHA2 - HTRA4 - TM2D2 - ADAM9 - ADAM32 - ADAM5p - ADAM3A - ADAM18 - ADAM2
TACC1; 8P11; Transforming, acidic coiled-coil containing protein 1
PLEKHA2; 8P11.23; Pleckstrin homology domain containing, family A member 2
HTRA4; 8P11.23; HtrA serine peptidase 4
TM2D2; 8P11.23; TM2 domain containing 2
ADAM9; 8P11.23; a disintegrin and metalloproteinase domain 9
ADAM32; 8p11.23; ADAM metalloproteinase domain 32
ADAM5P; 8p11.23; ADAM metallopeptidase domain 5 pseudogene
ADAM3A; 8p11.23; ADAM metallopeptidase domain 3A (Cyritestin 1)
ADAM18; 8p11.22; ADAM metallopeptidase domain 18
ADAM2; 8p11.22; ADAM metallopeptidase domain 2.
Note The ADAM9 gene, a member of the ADAM super-family have metalloprotease, integrin binding and cell adhesion capacities. It shown the metalloprotease domain cleaves insulin beta-chain, TNF-alpha, gelatin, beta-casein, fibronectin, as well as shedding of EGF, HB-EGF and FGFR2IIIB. The integrin domain mediates cellular adhesion through alpha6beta1 and alphavbeta5 integrins. The cytoplasmic tail of ADAM9 has been reported to interact with endophilin 1 (SH3GL2), SH3PX1 and mitotic arrest deficient 2beta. ADAM9 has implicated mediated by stress, such as oxidation during inflammation and cancer progression.

DNA/RNA

Note The ADAM9 gene transcript 2 isoforms of mRNA with altered splicing results the lost of exon 18 in the second isoform of ADAM9 mRNA and early stop codon.
 
  ADAM9 gene is located on chromosome 8p11.23 spread out on 108,276 deoxynucleotides contained 22 exons. The coding sequence of ADAM9 is 2460 nucleotides. Two isoforms reported, isoform 1 of ADAM9 carried full-length membrane bond ADAM9 and isoform 2 carried soluble form of ADAM9 (sADAM9). The sADAM9 is due to alternative splicing in which lost of exon 18 and results in early stop translation in exon 19.
Description ADAM9 gene extends 108,276 base pairs with 22 exons which gives rise to 2 different ADAM9 transcripts with differential splicing. The mRNA of ADAM9 isoform 1 is 4111 base pair and isoform 2 is 4005. ADAM9 isoform 2 lacks exon 18 of isoform 1 in the coding region, which results in a frameshift and an early stop codon. The isoform 2 lacks the c-terminal transmembrane and cytoplasmic domains and is a secreted form.
Transcription Isoform 1 mRNA of ADAM9 (NM_003816) has a size of 4111 bp, isoform 2 mRNA (NM_001005845) has a size of 4005 bp. ADAM9 mRNA is equally expressed in many tissue. Among cancer progression, ADAM9 mRNA is relatively highly expressed in prostate cancer and breast cancer. However, little is known of differential expression between different isoform of ADAM9.
Pseudogene No pseudogene has reported for ADAM9.

Protein

Note Two different isoform of ADAM9 was reported, the full length and soluble form of ADAM9. Recent report suggests promoter polymorphisms regulated ADAM9 transcription that play a protective role against Alzheimer's disease.
 
  Two isoforms of ADAM9 with their specific function. Soluble form of ADAM9 has function to active APP either on the same cell or neighbor cell.
Description The predicted molecular mass of ADAM9 is about 84 KDa. ADAM9 contained coding sequence of 2460 nucleotides which encoding amino acid of 819 residues. The full length of active ADAM9 contained several functional regions including metalloproteinase, disintegrin, cystein rich, EGF-like, transmembrane and cytoplasmic domains. The pro-domain of ADAM9 was removed by furin-type convertase during ADAM9 translocated onto membrane and become active form. Recent reports indicated soluble form of ADAM9 cloned from human cDNA library that showed increased of cancer invasion in malignant progression.
Expression ADAM9 is ubiquitously expressed. SAGE analyses of ADAM9 expression demonstrated that ADAM9 is expressed in the bone marrow, lymph node, brain, retina, heart, skin, muscle, lung, prostate, breast and placenta. Increased expression of ADAM9 was reported in several cancers, including gastric, breast, prostate, colon, and pancreatic cancers. Splicing alteration and lost of exon 18 of ADAM9 causes lost of transmembrane domain and early stop in soluble form of ADAM9.
Localisation Full length has N-terminal signal peptide and a single hydrophobic region predicted to be transmembrane domain. Hence, the full length of ADAM9 is localized to the plasma membrane. Soluble ADAM9 lack the transmembrane domain and cytoplasmic domain and to be released out of cell.
Function 1. Ectodomain shedding: Metalloproteinase domain of ADAM9 is zinc dependent. Metalloproteinase has been showed to involve ectodomain shedding (see table below). One such protein is the heparin-binding EGF-like growth factor (HB-EGF) and amyloid precursor protein (APP).
TABLE : Substrate and Peptide Sequence Cleaved
Substrate Peptide sequence cleaved (*: cleave site)
Amyloid precursor proteinEVHH*QKLVFFAE
TNF-aSPLA*QAVRS*SSR
P75 TNF receptorSMAPGAVH*LPQP
c-kit ligandLPPVA*A*S*SLRND
Insulin B ChainLVEALY*LVCGERGFFY*TPKA
HB-EGFGLSLPVE*NRLYTYD

2. Matrix Degradation: purified metalloproteinase domain of ADAM9 showed the ability to digest fibronectin, gelatin and beta-casein. Secreted form of ADAM9 showed the ability to digest laminin and promote cancer invasion.
3. Cell contact: ADAM9 specifically bind to integrin alpha6beta1, a laminin receptor, via disintegrin region of ADAM9 through non-RGD mechanism. ADAM9 also have been implicated in binding of avbeta5 in divalent cation dependent condition, suggests ADAM9 can function as adhesion molecule for cell-cell and cell-martrix interaction. Secreted form of ADAM9 binds directly to alpha6beta4 and alpha2beta1 integrin and ability to cleave laminin and promote cancer progression.
4. Cysteine-Rich domain: The ADAM Cysteine-rich domain is not found in other organisms, such as virus, archaeal, bacterial or plant. The function of cysteine-rich domain might involved in complement the binding ability of disintegrin-mediated interactions.
Homology The table below gives homology between the human ADAM9 and others organisms.
 

Mutations

Note Single nucleotide polymorphosim analyses of chromosome 8 demonstrated about 356 SNP in the chromosome 8p11.23. Most of them are located in intron of ADAM9. No mutation was reported in ADAM9 coding sequence. Recent evidence suggests promoter polymorphisms that may upregulate ADAM9 transcription, such as -1314C has higher of transcription activities.
 
  ADAM9 gene promoter region contained 4 polymorphisms: -542C/T, -600A/C, -963A/G and -1314T/C. 1314C showed higher ADAM9 transcription compared to 1314T.

Implicated in

Entity Prostate cancer
Note ADAM9 has been implicated in prostate cancer progression and the production of reactive oxygen species. Large cohort of clinic evaluation demonstrated ADAM9 is upregulated in prostate cancer in both mRNA and protein level. ADAM9 protein expression can be upregulated by androgen in AR-positive but not in AR-negative prostate cancer cells that is through downstream ROS as mediator to induce ADAM9 expression. ADAM9 protein expression is associated with shortened PSA-relapse-free survival in clinic evaluation.
  
Entity Pancreatic cancer
Note Pancreatic ductal adenocarcinomas showing increased of ADAM9 expression in microarray analyses and clinic evaluation that correlated with poor tumor differentiation and shorter overall survival rate.
  
Entity Breast cancer
Note ADAM9 expression is 24% positive in normal breast tissue and 66% positive in breast carcinomas. Western blot studies demonstrated multiform of ADAM9 were expressed in breast carcinoma. In addition, recent study demonstrated copy number abnormalities occurred in ADAM9 gene.
  
Entity Lung cancer
Note The increased of ADAM9 expression in lung cancer enhanced cell adhesion and invasion of non-small cell lung cancer through change adhesion properties and sensitivity to growth factors, and increase its capacity of brain metastasis.
  
Entity Renal cell carcinoma
Note ADAM9 was implicated increased expression in renal cell carcinoma and associated with tumor progression. It also showed higher of ADAM9 expression is associated with shorten patient survival rate.
  
Entity Alzheimer's disease
Note The amyloid precursor protein (APP) of Alzheimer's disease is a transmembrane protein processed via either the non-amyloidogenic or amyloidogenic pathways. In the non-amyloidogenic pathway, alpha-secretase cleaves APP within the Abeta peptide region releasing a large soluble fragment sAPPalpha that has neuroprotective properties. In the amyloidogenic pathway, beta-secretase and gamma-secretase sequentially cleave APP to generate the intact Abeta peptide, which is neurotoxic. In ADAM9 expression analyses showed increase in production of sAPPalpha upon phorbol ester treatment of cell that co-express of ADAM9 and APP. ADAM9 did not cleave at the Lys16-Leu17 bone but at the His14-Gln15 bone in the Abeta domain of APP cleave site. Hence, ADAM9 might play role in protective against sporadic Alzheimer's disease.
  

External links

Nomenclature
HGNC (Hugo)ADAM9   216
Cards
AtlasADAM9ID573ch8p11
Entrez_Gene (NCBI)ADAM9  8754  ADAM metallopeptidase domain 9
GeneCards (Weizmann)ADAM9
Ensembl (Hinxton)ENSG00000168615 [Gene_View]  chr8:38854505-38962779 [Contig_View]  ADAM9 [Vega]
ICGC DataPortalENSG00000168615
cBioPortalADAM9
AceView (NCBI)ADAM9
Genatlas (Paris)ADAM9
WikiGenes8754
SOURCE (Princeton)NM_001005845 NM_003816
Genomic and cartography
GoldenPath (UCSC)ADAM9  -  8p11.22   chr8:38854505-38962779 +  8p11.23   [Description]    (hg19-Feb_2009)
EnsemblADAM9 - 8p11.23 [CytoView]
Mapping of homologs : NCBIADAM9 [Mapview]
OMIM602713   612775   
Gene and transcription
Genbank (Entrez)AF495383 AK293257 AV708278 BC027996 BC126406
RefSeq transcript (Entrez)NM_001005845 NM_003816
RefSeq genomic (Entrez)AC_000140 NC_000008 NC_018919 NG_016335 NT_167187 NT_187577 NW_001839129 NW_004929337
Consensus coding sequences : CCDS (NCBI)ADAM9
Cluster EST : UnigeneHs.591852 [ NCBI ]
CGAP (NCI)Hs.591852
Alternative Splicing : Fast-db (Paris)GSHG0028963
Alternative Splicing GalleryENSG00000168615
Gene ExpressionADAM9 [ NCBI-GEO ]     ADAM9 [ SEEK ]   ADAM9 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13443 (Uniprot)
NextProtQ13443  [Medical]
With graphics : InterProQ13443
Splice isoforms : SwissVarQ13443 (Swissvar)
Catalytic activity : Enzyme3.4.24.- [ Enzyme-Expasy ]   3.4.24.-3.4.24.- [ IntEnz-EBI ]   3.4.24.- [ BRENDA ]   3.4.24.- [ KEGG ]   
Domaine pattern : Prosite (Expaxy)ADAM_MEPRO (PS50215)    DISINTEGRIN_1 (PS00427)    DISINTEGRIN_2 (PS50214)    EGF_2 (PS01186)    EGF_3 (PS50026)    ZINC_PROTEASE (PS00142)   
Domains : Interpro (EBI)ADAM_Cys-rich [organisation]   Blood-coag_inhib_Disintegrin [organisation]   Disintegrin_CS [organisation]   EG-like_dom [organisation]   EGF-like_CS [organisation]   MetalloPept_cat_dom [organisation]   Peptidase_M12B [organisation]   Peptidase_M12B_N [organisation]  
Related proteins : CluSTrQ13443
Domain families : Pfam (Sanger)ADAM_CR (PF08516)    Disintegrin (PF00200)    Pep_M12B_propep (PF01562)    Reprolysin (PF01421)   
Domain families : Pfam (NCBI)pfam08516    pfam00200    pfam01562    pfam01421   
Domain families : Smart (EMBL)ACR (SM00608)  DISIN (SM00050)  EGF (SM00181)  
DMDM Disease mutations8754
Blocks (Seattle)Q13443
PDB (SRS)1M1V   
PDB (PDBSum)1M1V   
PDB (IMB)1M1V   
PDB (RSDB)1M1V   
Human Protein AtlasENSG00000168615 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasQ13443
HPRD04091
IPIIPI00440932   IPI00440933   IPI01013119   IPI00793716   IPI00981311   IPI00947071   
Protein Interaction databases
DIP (DOE-UCLA)Q13443
IntAct (EBI)Q13443
FunCoupENSG00000168615
BioGRIDADAM9
InParanoidQ13443
Interologous Interaction database Q13443
IntegromeDBADAM9
STRING (EMBL)ADAM9
Ontologies - Pathways
Ontology : AmiGOactivation of MAPKK activity  metalloendopeptidase activity  metalloendopeptidase activity  protein kinase C binding  integrin binding  integrin binding  integrin binding  protein binding  collagen binding  extracellular space  extracellular space  cytoplasm  membrane protein ectodomain proteolysis  membrane protein ectodomain proteolysis  cell adhesion  cell-matrix adhesion  transforming growth factor beta receptor signaling pathway  transforming growth factor beta receptor signaling pathway  integrin-mediated signaling pathway  metallopeptidase activity  zinc ion binding  cell surface  response to manganese ion  integral component of membrane  basolateral plasma membrane  SH3 domain binding  SH3 domain binding  extracellular matrix disassembly  extracellular matrix organization  keratinocyte differentiation  collagen catabolic process  intrinsic component of external side of plasma membrane  cell adhesion mediated by integrin  positive regulation of cell adhesion mediated by integrin  cell-cell adhesion mediated by integrin  positive regulation of macrophage fusion  response to tumor necrosis factor  response to laminar fluid shear stress  monocyte activation  response to hydrogen peroxide  laminin binding  positive regulation of protein secretion  positive regulation of membrane protein ectodomain proteolysis  PMA-inducible membrane protein ectodomain proteolysis  PMA-inducible membrane protein ectodomain proteolysis  response to glucocorticoid  positive regulation of keratinocyte migration  response to calcium ion  cellular response to lipopolysaccharide  
Ontology : EGO-EBIactivation of MAPKK activity  metalloendopeptidase activity  metalloendopeptidase activity  protein kinase C binding  integrin binding  integrin binding  integrin binding  protein binding  collagen binding  extracellular space  extracellular space  cytoplasm  membrane protein ectodomain proteolysis  membrane protein ectodomain proteolysis  cell adhesion  cell-matrix adhesion  transforming growth factor beta receptor signaling pathway  transforming growth factor beta receptor signaling pathway  integrin-mediated signaling pathway  metallopeptidase activity  zinc ion binding  cell surface  response to manganese ion  integral component of membrane  basolateral plasma membrane  SH3 domain binding  SH3 domain binding  extracellular matrix disassembly  extracellular matrix organization  keratinocyte differentiation  collagen catabolic process  intrinsic component of external side of plasma membrane  cell adhesion mediated by integrin  positive regulation of cell adhesion mediated by integrin  cell-cell adhesion mediated by integrin  positive regulation of macrophage fusion  response to tumor necrosis factor  response to laminar fluid shear stress  monocyte activation  response to hydrogen peroxide  laminin binding  positive regulation of protein secretion  positive regulation of membrane protein ectodomain proteolysis  PMA-inducible membrane protein ectodomain proteolysis  PMA-inducible membrane protein ectodomain proteolysis  response to glucocorticoid  positive regulation of keratinocyte migration  response to calcium ion  cellular response to lipopolysaccharide  
Protein Interaction DatabaseADAM9
Wikipedia pathwaysADAM9
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)ADAM9
snp3D : Map Gene to Disease8754
SNP (GeneSNP Utah)ADAM9
SNP : HGBaseADAM9
Genetic variants : HAPMAPADAM9
Exome VariantADAM9
1000_GenomesADAM9 
ICGC programENSG00000168615 
Somatic Mutations in Cancer : COSMICADAM9 
CONAN: Copy Number AnalysisADAM9 
Mutations and Diseases : HGMDADAM9
Mutations and Diseases : intOGenADAM9
Genomic VariantsADAM9  ADAM9 [DGVbeta]
dbVarADAM9
ClinVarADAM9
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM602713    612775   
MedgenADAM9
GENETestsADAM9
Disease Genetic AssociationADAM9
Huge Navigator ADAM9 [HugePedia]  ADAM9 [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneADAM9
Homology/Alignments : Family Browser (UCSC)ADAM9
Phylogenetic Trees/Animal Genes : TreeFamADAM9
Chemical/Protein Interactions : CTD8754
Chemical/Pharm GKB GenePA24534
Clinical trialADAM9
Cancer Resource (Charite)ENSG00000168615
Other databases
Probes
Litterature
PubMed63 Pubmed reference(s) in Entrez
CoreMineADAM9
iHOPADAM9
OncoSearchADAM9

Bibliography

A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.
Izumi Y, Hirata M, Hasuwa H, Iwamoto R, Umata T, Miyado K, Tamai Y, Kurisaki T, Sehara-Fujisawa A, Ohno S, Mekada E.
EMBO J. 1998 Dec 15;17(24):7260-72.
PMID 9857183
 
Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta.
Nelson KK, Schlondorff J, Blobel CP.
Biochem J. 1999 Nov 1;343 Pt 3:673-80.
PMID 10527948
 
Intracellular processing of metalloprotease disintegrin ADAM12.
Cao Y, Kang Q, Zhao Z, Zolkiewska A.
J Biol Chem. 2002 Jul 19;277(29):26403-11. Epub 2002 May 8.
PMID 12000744
 
A secreted form of human ADAM9 has an alpha-secretase activity for APP.
Hotoda N, Koike H, Sasagawa N, Ishiura S.
Biochem Biophys Res Commun. 2002 May 3;293(2):800-5.
PMID 12054541
 
Gene expression profiles of microdissected ductal adenocarcinoma.
Grutzmann R, Foerder M, Alldinger I, Staub E, Brummendorf T, Ropcke S, Li X, Kristiansen G, Jesnowski R, Sipos B, Lohr M, Luttges J, Ockert D, Kloppel G, Saeger HD, Pilarsky C.
Virchows Arch. 2003 Oct;443(4):508-17. Epub 2003 Aug 27.
PMID 12942322
 
Oxidative and osmotic stress signaling in tumor cells is mediated by ADAM proteases and heparin-binding epidermal growth factor.
Fischer OM, Hart S, Gschwind A, Prenzel N, Ullrich A.
Mol Cell Biol. 2004 Jun;24(12):5172-83.
PMID 15169883
 
ADAM9 expression in pancreatic cancer is associated with tumour type and is a prognostic factor in ductal adenocarcinoma.
Grutzmann R, Luttges J, Sipos B, Ammerpohl O, Dobrowolski F, Alldinger I, Kersting S, Ockert D, Koch R, Kalthoff H, Schackert HK, Saeger HD, Kloppel G, Pilarsky C.
Br J Cancer. 2004 Mar 8;90(5):1053-8.
PMID 14997207
 
Overexpression of ADAM9 in non-small cell lung cancer correlates with brain metastasis.
Shintani Y, Higashiyama S, Ohta M, Hirabayashi H, Yamamoto S, Yoshimasu T, Matsuda H, Matsuura N.
Cancer Res. 2004 Jun 15;64(12):4190-6.
PMID 15205330
 
Gene expression analysis of pancreatic cell lines reveals genes overexpressed in pancreatic cancer.
Alldinger I, Dittert D, Peiper M, Fusco A, Chiappetta G, Staub E, Lohr M, Jesnowski R, Baretton G, Ockert D, Saeger HD, Grutzmann R, Pilarsky C.
Pancreatology. 2005;5(4-5):370-9. Epub 2005 Jun 23.
PMID 1598344
 
Developmental expression of metalloproteases ADAM 9, 10, and 17 becomes restricted to divergent pancreatic compartments.
Asayesh A, Alanentalo T, Khoo NK, Ahlgren U.
Dev Dyn. 2005 Apr;232(4):1105-14.
PMID 15739225
 
The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer.
Carl-McGrath S, Lendeckel U, Ebert M, Roessner A, Rocken C.
Int J Oncol. 2005 Jan;26(1):17-24.
PMID 15586220
 
A secreted form of ADAM9 promotes carcinoma invasion through tumor-stromal interactions.
Mazzocca A, Coppari R, De Franco R, Cho JY, Libermann TA, Pinzani M, Toker A.
Cancer Res. 2005 Jun 1;65(11):4728-38.
PMID 15930291
 
Critical function for ADAM9 in mouse prostate cancer.
Peduto L, Reuter VE, Shaffer DR, Scher HI, Blobel CP.
Cancer Res. 2005 Oct 15;65(20):9312-9.
PMID 16230393
 
Genomic and transcriptional aberrations linked to breast cancer pathophysiologies.
Chin K, DeVries S, Fridlyand J, Spellman PT, Roydasgupta R, Kuo WL, Lapuk A, Neve RM, Qian Z, Ryder T, Chen F, Feiler H, Tokuyasu T, Kingsley C, Dairkee S, Meng Z, Chew K, Pinkel D, Jain A, Ljung BM, Esserman L, Albertson DG, Waldman FM, Gray JW.
Cancer Cell. 2006 Dec;10(6):529-41.
PMID 17157792
 
Overexpression of ADAM9 enhances growth factor-mediated recycling of E-cadherin in human colon cancer cell line HT29 cells.
Hirao T, Nanba D, Tanaka M, Ishiguro H, Kinugasa Y, Doki Y, Yano M, Matsuura N, Monden M, Higashiyama S.
Exp Cell Res. 2006 Feb 1;312(3):331-9. Epub 2005 Dec 5.
PMID 16336960
 
Oxidative stress induces ADAM9 protein expression in human prostate cancer cells.
Sung SY, Kubo H, Shigemura K, Arnold RS, Logani S, Wang R, Konaka H, Nakagawa M, Mousses S, Amin M, Anderson C, Johnstone P, Petros JA, Marshall FF, Zhau HE, Chung LW.
Cancer Res. 2006 Oct 1;66(19):9519-26.
PMID 17018608
 
ADAMs in cancer cell proliferation and progression.
Mochizuki S, Okada Y.
Cancer Sci. 2007 May;98(5):621-8. Epub 2007 Mar 9.
PMID 17355265
 
Reactive oxygen species mediate androgen receptor- and serum starvation-elicited downstream signaling of ADAM9 expression in human prostate cancer cells.
Shigemura K, Sung SY, Kubo H, Arnold RS, Fujisawa M, Gotoh A, Zhau HE, Chung LW.
Prostate. 2007 May 15;67(7):722-31.
PMID 17342749
 
ADAM9 expression is a significant and independent prognostic marker of PSA relapse in prostate cancer.
Fritzsche FR, Jung M, Tolle A, Wild P, Hartmann A, Wassermann K, Rabien A, Lein M, Dietel M, Pilarsky C, Calvano D, Grutzmann R, Jung K, Kristiansen G.
Eur Urol. 2008 Nov;54(5):1097-106. Epub 2007 Nov 26.
PMID 18061337
 
ADAM9 is highly expressed in renal cell cancer and is associated with tumour progression.
Fritzsche FR, Wassermann K, Jung M, Tolle A, Kristiansen I, Lein M, Johannsen M, Dietel M, Jung K, Kristiansen G.
BMC Cancer. 2008 Jun 26;8:179.
PMID 18582378
 
Genomic aberrations in squamous cell lung carcinoma related to lymph node or distant metastasis.
Boelens MC, Kok K, van der Vlies P, van der Vries G, Sietsma H, Timens W, Postma DS, Groen HJ, van den Berg A.
Lung Cancer. 2009 Mar 24.
PMID 19324446
 
Expression of ADAMs ("a disintegrin and metalloprotease") in the human lung.
Dijkstra A, Postma DS, Noordhoek JA, Lodewijk ME, Kauffman HF, Ten Hacken NH, Timens W.
Virchows Arch. 2009 Apr;454(4):441-9. Epub 2009 Mar 3.
PMID 19255780
 
ADAM9 is involved in pathological retinal neovascularization.
Guaiquil V, Swendeman S, Yoshida T, Chavala S, Campochiaro PA, Blobel CP.
Mol Cell Biol. 2009 May;29(10):2694-703. Epub 2009 Mar 9.
PMID 19273593
 
EGFR and ADAMs cooperate to regulate shedding and endocytic trafficking of the desmosomal cadherin desmoglein 2.
Klessner JL, Desai BV, Amargo EV, Getsios S, Green KJ.
Mol Biol Cell. 2009 Jan;20(1):328-37. Epub 2008 Nov 5.
PMID 18987342
 
Up-regulated expression of ADAM17 in gastrointestinal stromal tumors: coexpression with EGFR and EGFR ligands.
Nakagawa M, Nabeshima K, Asano S, Hamasaki M, Uesugi N, Tani H, Yamashita Y, Iwasaki H.
Cancer Sci. 2009 Feb 27.
PMID 19298600
 
UV-induced EGFR signal transactivation is dependent on proligand shedding by activated metalloproteases in skin cancer cell lines.
Singh B, Schneider M, Knyazev P, Ullrich A.
Int J Cancer. 2009 Feb 1;124(3):531-9.
PMID 19003995
 
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Contributor(s)

Written04-2009Shian-Ying Sung
Center for Molecular Medicine and Graduate Institute of Cancer Biology, China Medical University and Hospital, Taichung, Taiwan

Citation

This paper should be referenced as such :
Sung, SY
ADAM9 (ADAM metallopeptidase domain 9 (meltrin gamma))
Atlas Genet Cytogenet Oncol Haematol. 2010;14(3):-.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/ADAM9ID573ch8p11.html

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indexed on : Fri Sep 5 10:47:37 CEST 2014

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